Article

Conserved water molecules as structural ligands modulating pathogenic variation in human protein binding sites

2026-04-03

Abstract excerpt

Conserved water molecules (CWMs) are tightly bound solvent molecules that occupy well-defined and recurrent positions in protein structures. Although they are known to influence protein stability, function, and ligand binding, their contribution to human genetic disease has remained largely unexplored. Here, we demonstrate that CWMs substantially contribute to the pathogenicity of single nucleotide polymorphisms (...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 2aeba810-3a94-5cab-b9d0-c6b7e8269a57
DOI: 10.64898/2026.04.01.715522

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Conserved water molecules as structural ligands modulating pathogenic variation in human protein binding sitesDOI 10.64898/2026.04.01.715522Read

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variants.Semantic proximity Read

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variantsSemantic proximity Read

Burden analysis of missense variants in 1,330 disease-associated genes on 3D provides insights into the mutation effectsSemantic proximity Read

Missense mutations: Backbone structure positional effectsSemantic proximity Read

Molecular mechanisms of disease-causing missense mutations.Semantic proximity Read

In-Silico Methods for Investigating the Effect of Single Nucleotide Polymorphisms on the Structure and Function of Proteins: A ReviewSemantic proximity Read

Accurate Identification and Mechanistic Evaluation of Pathogenic Missense Variants with <i>Rhapsody-2</i>Semantic proximity Read

Dissecting Mutational Allosteric Effects in Alkaline Phosphatases Associated with Different Hypophosphatasia Phenotypes: An Integrative Computational InvestigationSemantic proximity Read

Investigating the Impact of the Parkinson's-Associated GBA1 E326K Mutation on β-Glucocerebrosidase Dimerization and Interactome Dynamics Through an In Silico Approach.Semantic proximity Read

Molecular mechanisms of catalytic inhibition for active site mutations in glucose-6-phosphatase catalytic subunit 1 linked to glycogen storage diseaseSemantic proximity Read

Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties.Semantic proximity Read

The properties of human disease mutations at protein interfacesSemantic proximity Read